ID A0A0A1MTY9_9BACI Unreviewed; 709 AA.
AC A0A0A1MTY9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN Name=copB_1 {ECO:0000313|EMBL:CEI82997.1};
GN ORFNames=BN997_02886 {ECO:0000313|EMBL:CEI82997.1};
OS Oceanobacillus oncorhynchi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=545501 {ECO:0000313|EMBL:CEI82997.1, ECO:0000313|Proteomes:UP000040453};
RN [1] {ECO:0000313|EMBL:CEI82997.1, ECO:0000313|Proteomes:UP000040453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oc5 {ECO:0000313|EMBL:CEI82997.1,
RC ECO:0000313|Proteomes:UP000040453};
RA Urmite Genomes Urmite Genomes;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC ChEBI:CHEBI:456216; EC=7.2.2.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001390};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC ECO:0000256|RuleBase:RU362081}.
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DR EMBL; CDGG01000001; CEI82997.1; -; Genomic_DNA.
DR RefSeq; WP_042533148.1; NZ_JAUDBP010000008.1.
DR AlphaFoldDB; A0A0A1MTY9; -.
DR STRING; 545501.BN997_02886; -.
DR OrthoDB; 9813266at2; -.
DR Proteomes; UP000040453; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01512; ATPase-IB2_Cd; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000040453};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 76..97
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 103..121
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 142..161
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 167..184
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 351..370
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 658..677
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 683..706
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 709 AA; 77330 MW; A19A263FE3BF6793 CRC64;
MANHDSKKNN QSHSEHDGHK HHNHEHHNHE HHDHEHHSHD HREHHNHNGH DHSGHGHGGG
HAGHHEHMID DFKKRFWVSL VLAIPITYLS PMIQMLFNYE VNFTGNTIVL FLLSTIVFFY
GGKPFLLGAW DEIKTKTPGM MLLISLAIVT AYIYSTLTAF LIDGSDFYFE VATLIVIMLL
GHWVEMRSIM GASKALEELI KLMPKEAHKI DASGNIVEVS VEELHPGDEI LVKSGEKIPI
DGEIFEGEST VDESMLTGES VPVEKGPGMK AIGGAVNGEG VLKIKVNKIG NDTYLSQVIQ
LVSEAENTKS KAQGFANIAA KWLFYVAVVA GIITIAYWST TGDFEFALER MVTVLIIACP
HALGLAMPLV TSRSTSIAAK NGLLIRNRTP FENARKLDRV VFDKTGTLTE GNFGVTDIHP
SNNVSKDELV KLAYSVETQS DHPIAKGIVK EGKNRNLELY EVTNYRNLTG KGLTADVKGT
EIAVISPGAM KANNIDFDEE TYEKLAQQGK TVVFVLRDNV LQGMIALADI IRESSYEVIK
QLKDSGIETV MMTGDNNRVA NYVGEKLGLS KVISEVLPHD KSDNVKKLKE GGKKVAMIGD
GINDAPALAE ADLGIAIGAG TDVAIETADV VLVNSDPVDI LNILKLSKAS YRKMIQNLGW
AAGYNVIAIP LAAGVLYNVG IVITPAIGAA VMSLSTIICA INAQLLKID
//
